This instrumentation request is to purchase a new four-channel NMR console to be used in conjunction with an existing 11.7 T narrow bore super conducting magnet to create a new spectrometer capable of state-of-the-art NMR experiments on solid samples. Three new probes are requested: two magic angle spinning probes, one to spin at the highest speeds and one at intermediate speeds. This combination provides access to fundamentally different classes of experiments that permit study of both structure and dynamics for solid or solid-like samples. A static deuterium probe is requested that will provide opportunities to study local dynamics of specifically deuterated sites in proteins and membranes. The primary applications of this instrument will be in molecular biophysics for the study of fundamental protein and integral membrane protein dynamics and structure. This instrument will facilitate the study of proton-spin dynamics in protein systems that are critical to understanding the spin-physics of contrast development in MRI as well as the internal energy landscape in proteins as affected by local water- protein interactions. It will be applied to examine membrane docking of tandem C2 domains from synaptotagamin and to examine the problem of lipid de-mixing at the lipid-protein interface. It will facilitate studies of the dynamics and assembly of the Opa proteins in bilayers and provide structural and dynamical characterization of the key recognition sites for engulfment of bacteria by the host cells. It will facilitate studies of membrane-protein interactions and lipid order in membrane fusion problems including SNARE-mediated membrane fusion events that are important in understanding the infection process. The structure of the protein OmpA will be studied directly in lipid bilayers rather than in micelle supports to determine the most relevant structure and serve as a key test of optimal approaches to structure determination for membrane proteins.